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Database: UniProt
Entry: A0A226MVD0_CALSU
LinkDB: A0A226MVD0_CALSU
Original site: A0A226MVD0_CALSU 
ID   A0A226MVD0_CALSU        Unreviewed;      1095 AA.
AC   A0A226MVD0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=StAR-related lipid transfer protein 13 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASZ78_006263 {ECO:0000313|EMBL:OXB59080.1};
OS   Callipepla squamata (Scaled quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC   Callipepla.
OX   NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB59080.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB59080.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB59080.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB59080.1};
RA   Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA   Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA   Decker J.E., Seabury C.M.;
RT   "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT   of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT   Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT   Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXB59080.1}.
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DR   EMBL; MCFN01000421; OXB59080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226MVD0; -.
DR   STRING; 9009.A0A226MVD0; -.
DR   Proteomes; UP000198323; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd04375; RhoGAP_DLC1; 1.
DR   CDD; cd09592; SAM_DLC2; 1.
DR   CDD; cd08909; START_STARD13-like; 1.
DR   Gene3D; 1.10.287.2070; -; 1.
DR   Gene3D; 3.30.530.20; -; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   InterPro; IPR002913; START_lipid-bd_dom.
DR   PANTHER; PTHR12659; RHO-TYPE GTPASE ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR12659:SF6; STAR-RELATED LIPID TRANSFER PROTEIN 13; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF01852; START; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00234; START; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50848; START; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198323}.
FT   DOMAIN          646..850
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          881..1064
FT                   /note="START"
FT                   /evidence="ECO:0000259|PROSITE:PS50848"
FT   REGION          146..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1095 AA;  122694 MW;  0F72CAF0441AFCA8 CRC64;
     MGEDRTQGCS SFPVEVIVLV PCTKQLCEPW RPIDAEIEAK EACDWLRAAG FPQYAQLYED
     SQFPIDIAAV KKDHDFLDKD LVEPLCRRLN TLNKCASMKL DVNFQRKKSE DSDEEDLCAI
     SNKWTFQRTS RRWSRVDDID ALLHQSDRHG SSGDIKMKNT TSSESVLTDL SEPEVSSVHS
     ESSGGSDNRS QSGISSIARE TCNCSGQHES TLLPDLTVIN TTLSPKDNVK NEKPTRTKAK
     TFLKRMETLK AKGVHGKLKG SGRAGPLEIS GPVLQREPKS LKDMHCVQIV NGDLQNLAQD
     SGKRGLSFSA KSSSESSQSE NSSSGVSTPC LKERKCHEAN KRGGMYLEDL DVLAGTALRQ
     VVDQNRKNEF HSQENLVVHI PKDHKPGTFP KALSIESLSP TDNSNGVNWR TGSISLGKQN
     CSTPKETGLM ACCPKESRMS IYDNVPGSHL YASTGDLLDL EKDVLFPHLD DILQHVNGLR
     DVVDGWSKNV LPGLPVDDVS VRESPSLPFQ SPTQITLDFE GNSVSDGRTT PSDMERDGTS
     LNESEATGVR ERRDSGVGAS LTRPSRQLRW HSFQISHHLS HSIASLHISN QSAAQLNLLQ
     KFSLLRLTAI MEKYSMSNKH GWTWSVPKFM KRMKVPDYKD KNVFGVPLIV HVQRTGQPLP
     QSIQQALHYL RGNCLDQVGL FRKSGVKSRI QALRQMNESS PENVNYEDQS AYDVADMVKQ
     FFRDLPEPLL TSKLGETFLH IYQYVPKEQR LQAVQAAIML MADENREVLQ TLLCFLSDVT
     SVEENQMTPM NIAVCLAPSL FHLNIVKKES SPRVIQKKYA TGKPDQKDLS ENLAATQGLA
     HMIMECNKLF EVPHEMVTQS RNSYIDAEVH SPTLDELGKQ VEEEGGNYQM YLESLMQNLH
     KEAKEKFKGW VTCSSMENTE LAYKKVGDGN PLRLWKASVE VEAPPSVVLN RVLRERHLWD
     EDFLQWKVVE SLDKQTEVYQ YVLNSMAPHP VRDFVVLRTW RTDLPRGTCM LVAISVEHEE
     APLMGAVRAI VMDSQYLIEP CGSGKARLTH ICRIDLKGHS PEWYNKGFGH LCAAEVARIR
     NSFQPLIAEG PETKI
//
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